Biochemistry

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Biochemistry

© All Rights Reserved

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For many enzymes, the rate of

catalysis, V, varies with the

substrate concentration, [S].

V is defined as the number of

moles of product formed per

second.

At a fixed concentration of

enzyme, V is almost linearly

proportional to the initial

increasing concentration of [S].

At very high [S], V is independent

of [S].

(Leonor) Michaelis and (Maud) Menten devised a model for the kinetics of enzymecatalyzed reactions.

The model proposed is the one that accounts for the kinetic properties of many

enzymes:

An enzyme, E, combines with S to form an ES complex, with a rate constant k1. The ES

complex has two possible fates. It can dissociate to E and S, with a rate constant of k-1,

or it can proceed to form product, P, with a rate constant k2.

Michaelis and Menten made a derivation of these kinetic characteristics to arrive at the

Michaelis-Menten Equation:

Vinit =

Vmax [S]

KM + [S]

Mi chael is-Menten

equation

For an enzyme-catalyzed reaction

E + S

k1

k-1

ES

k2

given by these equations

rate of formation of ES = k 1 [E][S]

rate of breakdown of ES = k

-1 [ES]

k1 [E][S] = k-1[ES] + k 2[ES]

+ k 2[ES]

When the steady state is reached, the concentration

of free enzyme is the total less that bound in ES

[E] = [E]T - [ES]

collecting all rate constants in one term gives

([E]T - [ES]) [S]

[ES]

k-1 + k2

= KM

k1

It is now possible to solve for the concentration of the

enzyme-substrate complex, [ES]

[E]T [S] - [ES][S]

= KM

[ES]

[E]T [S] - [ES][S] = KM [ES]

[E]T [S] = [ES](K M + [S])

Or alternatively

[E]T [S]

[ES] =

KM + [S]

In the initial stages, formation of product depends only on the

rate of breakdown of ES

Vinit = k 2 [ES]

k 2[E]T [S]

=

KM + [S]

saturated with substrate [ES] = [E]T

Substituting k2[E]T = Vmax into the top equation gives

Vinit =

Vmax [S]

KM + [S]

Mi chael is-Menten

equation

Initial concentration of substrate at Vmax or at half saturation of E

with S

Ratio of the constants for the breakdown of ES to constants of its

[E]T [S] - [ES][S]

formation:

= KM

[ES]

[E]T [S] - [ES][S] = KM [ES]

[E]T [S] = [ES](K M + [S])

therefore KM = k-1/k1

The lower the KM value, the more affinity has the enzyme for its

substrate

The [S]=

Meaning

KM orreduces

the Michaelis

constant

When

KM, the of

equation

to

V=

Vmax [S]

KM + [S]

Vmax [S]

[S] + [S]

Vmax

2

It is difficult to determine Vmax experimentally

Vmax

[S]

The equation

of

Michaelis

and Menten

is for

V=

(an

equation

fora ahyperbola

hyperbola)

KM + [S]

straight line by taking the reciprocal of each side

KM + [S]

Vmax [S]

KM

+

=

Vmax [S]

1

V

1

V

KM

+ 1

=

Vmax [S]

Vmax

[S]

Vmax [S]

Lineweaver-Burk Plot

1 form

1 + b, and is the

The Lineweaver-Burke

the

y = mx

1 = KMplot has

+

line

Vmax

[S]

V

max

a plot of 1/V versus 1/[S] will give a straight line with slope of

KM/Vmax and y intercept of 1/Vmax

such a plot is known as a Lineweaver-Burk double reciprocal

plot

Double reciprocal plots can easily be understood and provide

recognizable pattern for the study of ENZYME INHIBITION

KLineweaver-Burk

M is the

dissociation

constant for ES; the

greater the value of

KM, the less tightly S

is bound to E

number

Plot (Contd)

Turnover Numbers

Vmax is related to the turnover number of enzyme:also

called kmax

cat

[ET ]

per mole of enzyme per unit of time

Enzyme Inhibition

Reversible inhibitor: a substance that binds to an enzyme to inhibit it,

but can be released

blocks access to it by substrate

noncompetitive inhibitor: binds to a site other than the active

site; inhibits the enzyme by changing its conformation

Irreversible inhibitor: a substance that causes inhibition that cannot be

reversed

on the enzyme

Competitive Inhibition

Substrate must compete with inhibitor for the active site;

more substrate is required to reach a given reaction

velocity

EI

I + E + S

ES

P

EI

KI =

[E][I]

[EI]

Competitive Inhibition

Competitive

Inhibition

No inhibiti

on

y =

KM

Vmax

m

1

V

1

S

1

Vmax

b

1

V

KM

Vmax

1 +

[I]

KI

1

S

1

Vmax

b

slope (and the x intercept) changes but the y intercept does not

change

+S

Several equilibria are involved

E

-I

ES

-S

+I

-I

+S

EI

+I

ESI

-S

V

max

Vmax

1 + [I]/KI

E + P

Inhibition

Because the inhibitor does not interfere with binding of

substrate to the active site, KM is unchanged

Increasing substrate concentration cannot overcome

noncompetitive

inhibition

No inhibiti

on

1 = KM 1 + 1

V

S

Vmax

Vmax

y =

m x + b

In the presence of a noncompetitive inhibitor

1

V

KM

Vmax

1 +

m

[I]

KI

1

S

+

+

1

Vmax

1 +

b

[I]

KI

Inhibition (Contd)

Uncompetitive- inhibitor can bind to the ES complex but not to free

E. Vmax decreases and KM decreases.

S and vice versa.

Uncompetitive Inhibition

Uncompetitive Inhibition

Summary

Effects Type

of reversible

inhibitors on kinetic

constants

of Inhibitor

Effect

Competitive (I binds to E only)

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